Study on interaction between curcumin and pepsin by spectroscopic and docking methods.

摘要: Abstract The interaction between curcumin and pepsin was investigated by fluorescence, synchronous UV–vis absorption, circular dichroism (CD), molecular docking. Under physiological pH value in stomach, the fluorescence of can be quenched effectively via a combined quenching process. Binding constant ( K ) binding site number n to were obtained. According theory Forster's non-radiation energy transfer, distance r found 2.45 nm within curcumin–pepsin complex, which implies that transfer occurs pepsin, leading fluorescence. Fluorescence experiments also suggest is located more closely tryptophan residues than tyrosine residues. CD spectra together with absorbance studies show results extension peptide strands loss some β-sheet structures. Thermodynamic parameters calculated from constants at different temperatures reveal hydrophobic force plays major role stabilizing complex. In addition, docking support above experimental findings possible hydrogen bonds Thr-77, Thr-218, Glu-287 help further stabilize